Protein–protein interaction
Def-
Protein–protein interactions (PPIs) are the physical contacts of high specificity
established between two or more protein molecules as a result of biochemical events steered by
electrostatic forces including the hydrophobic effect.
Proteins have to interact with each other to carry out biochemical functions. Thus,
mapping out protein–protein interactions is another important aspect of proteomics. Inter protein
interactions include strong interactions that allow formation of stable complexes and weaker
ones that exist transiently. Proteins involved in forming complexes are generally more tightly co
regulated in expression than those involved in transient interactions.
Protein–protein interaction Database:-
To make this information more readily available, a number of publicly available
databases have set out to collect and store protein–protein interaction data. Protein–protein
interactions have been retrieved from major databases, integrated and the results compared.
BIND - Biomolecular Interaction Network Database
BioGRID- A Biological General Repository for Interaction Datasets (Samuel Lunenfeld
Research Institute)
DIP - Database of Interacting Proteins
IntAct molecular interaction database: a central, standards-compliant repository of
molecular interactions, including protein–protein, protein– small molecule and protein–
nucleic acid interactions.
STRING: STRING is a database of known and predicted protein-protein interactions.
(EMBL)
MINT: Molecular Interaction database
PRIDE- PRoteomics IDEntifications database
HPRD- the Human Protein Reference Database
MIPS- The Munich Information Center for Protein Sequences
.
BIND - The Biomolecular Interaction Network Database (http://bind.ca)
- The Biomolecular Interaction Network Database (BIND: http://bind.ca) archives
biomolecular interaction, complex and pathway information.
- A web based system is available to query, view and submit records.
- BIND continues to grow with the addition of individual submissions as well as interaction
data from the PDB and a number of large-scale interaction and complex mapping
experiments using yeast two hybrid, mass spectrometry, genetic interactions and phage
display.
We have developed a new graphical analysis tool that provides users with a view of the
domain composition of proteins in interaction and complex records to help relate functional
domains to protein interactions.
- An interaction network clustering tool has also been developed to help focus on regions of
interest.
- Continued input from users has helped further mature the BIND data specification, which
now includes the ability to store detailed information about genetic interactions.
- The BIND data specification is available as ASN.1 and XML DTD.
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